data_5107 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignments of the 1H, 13C, and 15N resonances of the substrate-binding SSD domain from Lon protease ; _BMRB_accession_number 5107 _BMRB_flat_file_name bmr5107.str _Entry_type original _Submission_date 2001-08-15 _Accession_date 2001-08-15 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Smith Catherine K. . 2 Wohnert Jens . . 3 Sauer Robert T. . 4 Schwalbe Harald . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 541 "13C chemical shifts" 421 "15N chemical shifts" 98 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-09-12 update author 'Correction of 3 chemical shifts' 2001-08-28 original author 'Original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Assignments of the 1H, 13C, and 15N resonances of the substrate-binding SSD domain from Lon protease ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21682385 _PubMed_ID 11824761 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Smith Catherine K. . 2 Wohnert Jens . . 3 Sauer Robert T. . 4 Schwalbe Harald . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 21 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 387 _Page_last 388 _Year 2001 _Details . loop_ _Keyword 'Heteronuclear NMR' 'Resonance assignment' 'Lon protease' 'Clp/Hsp100 family' stop_ save_ ################################## # Molecular system description # ################################## save_system_Lon_SSD _Saveframe_category molecular_system _Mol_system_name 'Sensor and Substrate Binding Domain from Lon (La) Protease (E. coli)' _Abbreviation_common 'Lon SSD' _Enzyme_commission_number 3.4.21.53 loop_ _Mol_system_component_name _Mol_label 'Lon SSD' $Lon_SSD stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'substrate binding' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Lon_SSD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Lon (La) protease SSD' _Abbreviation_common 'Lon SSD' _Molecular_mass 11710 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 101 _Mol_residue_sequence ; MRLSGYTEDEKLNIAKRHLL PKQIERNALKKGELTVDDSA IIGIIRYYTREAGVRGLERE ISKLCRKAVKQLLLDKSLKH IEINGDNLHDYLGVQRFDYG R ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ARG 3 LEU 4 SER 5 GLY 6 TYR 7 THR 8 GLU 9 ASP 10 GLU 11 LYS 12 LEU 13 ASN 14 ILE 15 ALA 16 LYS 17 ARG 18 HIS 19 LEU 20 LEU 21 PRO 22 LYS 23 GLN 24 ILE 25 GLU 26 ARG 27 ASN 28 ALA 29 LEU 30 LYS 31 LYS 32 GLY 33 GLU 34 LEU 35 THR 36 VAL 37 ASP 38 ASP 39 SER 40 ALA 41 ILE 42 ILE 43 GLY 44 ILE 45 ILE 46 ARG 47 TYR 48 TYR 49 THR 50 ARG 51 GLU 52 ALA 53 GLY 54 VAL 55 ARG 56 GLY 57 LEU 58 GLU 59 ARG 60 GLU 61 ILE 62 SER 63 LYS 64 LEU 65 CYS 66 ARG 67 LYS 68 ALA 69 VAL 70 LYS 71 GLN 72 LEU 73 LEU 74 LEU 75 ASP 76 LYS 77 SER 78 LEU 79 LYS 80 HIS 81 ILE 82 GLU 83 ILE 84 ASN 85 GLY 86 ASP 87 ASN 88 LEU 89 HIS 90 ASP 91 TYR 92 LEU 93 GLY 94 VAL 95 GLN 96 ARG 97 PHE 98 ASP 99 TYR 100 GLY 101 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1QZM "Alpha-Domain Of Atpase" 93.07 94 100.00 100.00 3.91e-59 DBJ BAB33916 "endopeptidase La [Escherichia coli O157:H7 str. Sakai]" 100.00 784 99.01 100.00 8.82e-60 DBJ BAE76219 "DNA-binding ATP-dependent protease La [Escherichia coli str. K-12 substr. W3110]" 100.00 784 99.01 100.00 8.91e-60 DBJ BAG75989 "ATP-dependent protease [Escherichia coli SE11]" 100.00 784 99.01 100.00 8.91e-60 DBJ BAH62055 "DNA-binding ATP-dependent protease La/heat shock K-protein [Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044]" 100.00 820 97.03 99.01 4.12e-58 DBJ BAI23813 "DNA-binding ATP-dependent protease La [Escherichia coli O26:H11 str. 11368]" 100.00 784 99.01 100.00 8.91e-60 EMBL CAD08909 "Lon protease [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 784 98.02 99.01 5.58e-59 EMBL CAP74973 "ATP-dependent protease La [Escherichia coli LF82]" 100.00 784 99.01 100.00 8.91e-60 EMBL CAQ30912 "DNA-binding, ATP-dependent protease La [Escherichia coli BL21(DE3)]" 100.00 784 99.01 100.00 8.91e-60 EMBL CAQ90073 "DNA-binding ATP-dependent protease La [Escherichia fergusonii ATCC 35469]" 100.00 784 99.01 100.00 1.00e-59 EMBL CAQ97315 "DNA-binding ATP-dependent protease La [Escherichia coli IAI1]" 100.00 784 99.01 100.00 8.91e-60 GB AAA16837 "ATP-dependent protease [Escherichia coli str. K-12 substr. W3110]" 100.00 784 99.01 100.00 1.13e-59 GB AAA24079 "ATP-dependent proteinase (lon) [Escherichia coli]" 100.00 797 99.01 100.00 1.16e-59 GB AAB40195 "ATP-dependent protease LA [Escherichia coli]" 100.00 799 99.01 100.00 8.47e-60 GB AAC36871 "lon protease [Escherichia coli]" 100.00 784 99.01 100.00 8.91e-60 GB AAC73542 "DNA-binding ATP-dependent protease La [Escherichia coli str. K-12 substr. MG1655]" 100.00 784 99.01 100.00 8.91e-60 PIR AE0558 "Lon protease [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 784 98.02 99.01 5.58e-59 PRF 2004285A "lon protease" 100.00 784 99.01 100.00 8.91e-60 REF NP_286181 "DNA-binding ATP-dependent protease La [Escherichia coli O157:H7 str. EDL933]" 100.00 799 99.01 100.00 7.75e-60 REF NP_308520 "DNA-binding ATP-dependent protease La [Escherichia coli O157:H7 str. Sakai]" 100.00 784 99.01 100.00 8.82e-60 REF NP_414973 "DNA-binding ATP-dependent protease La [Escherichia coli str. K-12 substr. MG1655]" 100.00 784 99.01 100.00 8.91e-60 REF NP_455047 "Lon protease [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 784 98.02 99.01 5.58e-59 REF NP_459446 "Lon protease [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 784 98.02 99.01 5.36e-59 SP P0A9M0 "RecName: Full=Lon protease; AltName: Full=ATP-dependent protease La [Escherichia coli K-12]" 100.00 784 99.01 100.00 8.91e-60 SP P0A9M1 "RecName: Full=Lon protease; AltName: Full=ATP-dependent protease La [Escherichia coli CFT073]" 100.00 784 99.01 100.00 8.91e-60 SP Q32JJ5 "RecName: Full=Lon protease; AltName: Full=ATP-dependent protease La [Shigella dysenteriae Sd197]" 100.00 812 99.01 100.00 9.30e-60 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $Lon_SSD 'E. coli' 562 Eubacteria . Escherichia coli K12 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $Lon_SSD 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) pLysS stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Lon_SSD 3.0 mM [U-15N] stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Lon_SSD 3.0 mM '[U-15N; U-13C]' stop_ save_ ############################ # Computer software used # ############################ save_NMRpipe _Saveframe_category software _Name NMRpipe _Version 1.8 loop_ _Task 'processing spectra' stop_ _Details . save_ save_nmrView _Saveframe_category software _Name nmrView _Version 1.8 loop_ _Task 'analyzing spectra' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityInova _Field_strength 750 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC' _Sample_label . save_ save_13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '13C HSQC' _Sample_label . save_ save_HCCH-TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HCC(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name HCC(CO)NH _Sample_label . save_ save_CC(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name CC(CO)NH _Sample_label . save_ save_HBHA(CO)NH_9 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HCC(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name CC(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 5.3 0.1 n/a temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Lon SSD' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 MET HA H 4.117 0.03 1 2 . 1 MET HB2 H 2.098 0.03 2 3 . 1 MET HG2 H 2.572 0.03 2 4 . 1 MET HG3 H 2.405 0.03 2 5 . 1 MET HE H 2.633 0.03 1 6 . 1 MET CA C 54.860 0.08 1 7 . 1 MET CB C 32.850 0.08 1 8 . 1 MET CG C 30.428 0.08 1 9 . 1 MET CE C 17.902 0.08 1 10 . 2 ARG H H 8.713 0.03 1 11 . 2 ARG HA H 4.390 0.03 1 12 . 2 ARG HB2 H 1.808 0.03 2 13 . 2 ARG HG2 H 1.596 0.03 2 14 . 2 ARG HG3 H 1.531 0.03 2 15 . 2 ARG HD2 H 3.171 0.03 2 16 . 2 ARG HD3 H 3.133 0.03 2 17 . 2 ARG CA C 56.009 0.08 1 18 . 2 ARG CB C 30.904 0.08 1 19 . 2 ARG CG C 27.056 0.08 1 20 . 2 ARG CD C 43.215 0.08 1 21 . 2 ARG N N 124.738 0.08 1 22 . 3 LEU H H 8.596 0.03 1 23 . 3 LEU HA H 4.313 0.03 1 24 . 3 LEU HB2 H 1.629 0.03 2 25 . 3 LEU HB3 H 1.568 0.03 2 26 . 3 LEU HG H 1.621 0.03 1 27 . 3 LEU HD1 H 0.895 0.03 1 28 . 3 LEU HD2 H 0.850 0.03 1 29 . 3 LEU C C 176.180 0.08 1 30 . 3 LEU CA C 55.849 0.08 1 31 . 3 LEU CB C 42.209 0.08 1 32 . 3 LEU CG C 26.908 0.08 1 33 . 3 LEU CD1 C 24.890 0.08 2 34 . 3 LEU CD2 C 23.597 0.08 2 35 . 3 LEU N N 125.230 0.08 1 36 . 4 SER H H 8.078 0.03 1 37 . 4 SER HA H 4.376 0.03 1 38 . 4 SER HB2 H 3.896 0.03 2 39 . 4 SER HB3 H 3.820 0.03 2 40 . 4 SER C C 177.548 0.08 1 41 . 4 SER CA C 59.368 0.08 1 42 . 4 SER CB C 63.804 0.08 1 43 . 4 SER N N 114.434 0.08 1 44 . 5 GLY H H 8.005 0.03 1 45 . 5 GLY HA2 H 4.109 0.03 2 46 . 5 GLY HA3 H 3.766 0.03 2 47 . 5 GLY C C 174.519 0.08 1 48 . 5 GLY CA C 44.645 0.08 1 49 . 5 GLY N N 109.611 0.08 1 50 . 6 TYR H H 8.013 0.03 1 51 . 6 TYR HA H 4.984 0.03 1 52 . 6 TYR HB2 H 3.246 0.03 2 53 . 6 TYR HB3 H 2.470 0.03 2 54 . 6 TYR C C 173.836 0.08 1 55 . 6 TYR CA C 57.199 0.08 1 56 . 6 TYR CB C 41.655 0.08 1 57 . 6 TYR N N 119.397 0.08 1 58 . 7 THR H H 9.361 0.03 1 59 . 7 THR HA H 4.487 0.03 1 60 . 7 THR HB H 4.773 0.03 1 61 . 7 THR HG2 H 1.369 0.03 1 62 . 7 THR C C 177.841 0.08 1 63 . 7 THR CA C 60.795 0.08 1 64 . 7 THR CB C 70.996 0.08 1 65 . 7 THR CG2 C 21.787 0.08 1 66 . 7 THR N N 114.033 0.08 1 67 . 8 GLU H H 9.040 0.03 1 68 . 8 GLU HA H 3.812 0.03 1 69 . 8 GLU HB2 H 2.046 0.03 2 70 . 8 GLU HB3 H 2.205 0.03 2 71 . 8 GLU HG2 H 2.313 0.03 2 72 . 8 GLU HG3 H 2.106 0.03 2 73 . 8 GLU C C 175.594 0.08 1 74 . 8 GLU CA C 61.362 0.08 1 75 . 8 GLU CB C 29.957 0.08 1 76 . 8 GLU CG C 38.006 0.08 1 77 . 8 GLU N N 121.641 0.08 1 78 . 9 ASP H H 8.343 0.03 1 79 . 9 ASP HA H 4.335 0.03 1 80 . 9 ASP HB2 H 2.563 0.03 2 81 . 9 ASP HB3 H 2.455 0.03 2 82 . 9 ASP C C 177.938 0.08 1 83 . 9 ASP CA C 57.361 0.08 1 84 . 9 ASP CB C 40.931 0.08 1 85 . 9 ASP N N 116.143 0.08 1 86 . 10 GLU H H 7.800 0.03 1 87 . 10 GLU HA H 4.024 0.03 1 88 . 10 GLU HB2 H 1.874 0.03 2 89 . 10 GLU HB3 H 2.553 0.03 2 90 . 10 GLU HG2 H 2.337 0.03 2 91 . 10 GLU HG3 H 2.502 0.03 2 92 . 10 GLU C C 179.208 0.08 1 93 . 10 GLU CA C 59.086 0.08 1 94 . 10 GLU CB C 29.724 0.08 1 95 . 10 GLU CG C 37.434 0.08 1 96 . 10 GLU N N 120.215 0.08 1 97 . 11 LYS H H 8.465 0.03 1 98 . 11 LYS HA H 3.480 0.03 1 99 . 11 LYS HB2 H 2.078 0.03 2 100 . 11 LYS HB3 H 1.393 0.03 2 101 . 11 LYS HG2 H 0.764 0.03 2 102 . 11 LYS HG3 H 1.810 0.03 2 103 . 11 LYS HD2 H 1.608 0.03 2 104 . 11 LYS HD3 H 1.801 0.03 2 105 . 11 LYS HE2 H 3.290 0.03 2 106 . 11 LYS C C 180.991 0.08 1 107 . 11 LYS CA C 60.894 0.08 1 108 . 11 LYS CB C 34.386 0.08 1 109 . 11 LYS CG C 27.094 0.08 4 110 . 11 LYS CD C 31.758 0.08 4 111 . 11 LYS CE C 41.603 0.08 1 112 . 11 LYS N N 119.175 0.08 1 113 . 12 LEU H H 8.410 0.03 1 114 . 12 LEU HA H 3.854 0.03 1 115 . 12 LEU HB2 H 2.065 0.03 2 116 . 12 LEU HB3 H 1.410 0.03 2 117 . 12 LEU HG H 1.481 0.03 1 118 . 12 LEU HD1 H 0.890 0.03 1 119 . 12 LEU HD2 H 0.901 0.03 1 120 . 12 LEU C C 177.841 0.08 1 121 . 12 LEU CA C 58.544 0.08 1 122 . 12 LEU CB C 41.567 0.08 1 123 . 12 LEU CG C 27.017 0.08 1 124 . 12 LEU CD1 C 25.735 0.08 2 125 . 12 LEU CD2 C 24.280 0.08 2 126 . 12 LEU N N 120.332 0.08 1 127 . 13 ASN H H 7.651 0.03 1 128 . 13 ASN HA H 4.407 0.03 1 129 . 13 ASN HB2 H 2.851 0.03 2 130 . 13 ASN HB3 H 2.732 0.03 2 131 . 13 ASN C C 178.036 0.08 1 132 . 13 ASN CA C 57.047 0.08 1 133 . 13 ASN CB C 38.914 0.08 1 134 . 13 ASN N N 116.496 0.08 1 135 . 14 ILE H H 8.362 0.03 1 136 . 14 ILE HA H 3.697 0.03 1 137 . 14 ILE HB H 1.688 0.03 1 138 . 14 ILE HG12 H 0.916 0.03 2 139 . 14 ILE HG13 H 1.695 0.03 2 140 . 14 ILE HG2 H 0.899 0.03 1 141 . 14 ILE HD1 H 0.216 0.03 1 142 . 14 ILE C C 177.645 0.08 1 143 . 14 ILE CA C 65.706 0.08 1 144 . 14 ILE CB C 38.589 0.08 1 145 . 14 ILE CG1 C 29.763 0.08 2 146 . 14 ILE CG2 C 17.234 0.08 2 147 . 14 ILE CD1 C 13.210 0.08 1 148 . 14 ILE N N 121.208 0.08 1 149 . 15 ALA H H 9.006 0.03 1 150 . 15 ALA HA H 3.930 0.03 1 151 . 15 ALA HB H 1.555 0.03 1 152 . 15 ALA C C 179.892 0.08 1 153 . 15 ALA CA C 55.822 0.08 1 154 . 15 ALA CB C 19.032 0.08 1 155 . 15 ALA N N 123.593 0.08 1 156 . 16 LYS H H 8.440 0.03 1 157 . 16 LYS HA H 3.914 0.03 1 158 . 16 LYS HB2 H 1.886 0.03 2 159 . 16 LYS HB3 H 1.758 0.03 2 160 . 16 LYS HG2 H 1.633 0.03 2 161 . 16 LYS HG3 H 1.387 0.03 2 162 . 16 LYS HD2 H 1.772 0.03 2 163 . 16 LYS HE2 H 2.961 0.03 2 164 . 16 LYS HE3 H 2.858 0.03 2 165 . 16 LYS CA C 60.133 0.08 1 166 . 16 LYS CB C 32.677 0.08 1 167 . 16 LYS CG C 25.273 0.08 4 168 . 16 LYS CD C 29.948 0.08 4 169 . 16 LYS CE C 41.275 0.08 1 170 . 16 LYS N N 115.301 0.08 1 171 . 17 ARG H H 8.388 0.03 1 172 . 17 ARG HA H 4.201 0.03 1 173 . 17 ARG HB2 H 1.641 0.03 2 174 . 17 ARG HB3 H 1.493 0.03 2 175 . 17 ARG HG2 H 1.650 0.03 2 176 . 17 ARG HG3 H 1.493 0.03 2 177 . 17 ARG HD2 H 3.057 0.03 2 178 . 17 ARG C C 178.232 0.08 1 179 . 17 ARG CA C 57.368 0.08 1 180 . 17 ARG CB C 30.976 0.08 1 181 . 17 ARG CG C 27.619 0.08 1 182 . 17 ARG CD C 43.095 0.08 1 183 . 17 ARG N N 113.414 0.08 1 184 . 18 HIS H H 7.936 0.03 1 185 . 18 HIS HA H 5.065 0.03 1 186 . 18 HIS HB2 H 3.255 0.03 2 187 . 18 HIS HB3 H 3.179 0.03 2 188 . 18 HIS C C 176.962 0.08 1 189 . 18 HIS CA C 56.779 0.08 1 190 . 18 HIS CB C 32.189 0.08 1 191 . 18 HIS N N 113.026 0.08 1 192 . 19 LEU H H 8.132 0.03 1 193 . 19 LEU HA H 4.115 0.03 1 194 . 19 LEU HB2 H 1.981 0.03 2 195 . 19 LEU HB3 H 1.378 0.03 2 196 . 19 LEU HG H 1.346 0.03 1 197 . 19 LEU HD1 H 0.799 0.03 1 198 . 19 LEU HD2 H 0.783 0.03 1 199 . 19 LEU C C 175.985 0.08 1 200 . 19 LEU CA C 58.590 0.08 1 201 . 19 LEU CB C 42.650 0.08 1 202 . 19 LEU CG C 30.295 0.08 1 203 . 19 LEU CD1 C 25.764 0.08 2 204 . 19 LEU CD2 C 20.879 0.08 2 205 . 19 LEU N N 116.762 0.08 2 206 . 20 LEU H H 9.451 0.03 1 207 . 20 LEU HA H 4.194 0.03 1 208 . 20 LEU HB2 H 1.534 0.03 1 209 . 20 LEU HB3 H 2.00 0.03 1 210 . 20 LEU HG H 1.497 0.03 1 211 . 20 LEU HD1 H 0.878 0.03 1 212 . 20 LEU HD2 H 0.787 0.03 1 213 . 20 LEU C C 178.134 0.08 1 214 . 20 LEU CA C 59.743 0.08 1 215 . 20 LEU CB C 39.402 0.08 1 216 . 20 LEU CG C 27.75 0.08 1 217 . 20 LEU CD1 C 25.623 0.08 1 218 . 20 LEU CD2 C 24.147 0.08 1 219 . 20 LEU N N 117.983 0.08 1 220 . 21 PRO HA H 4.156 0.03 1 221 . 21 PRO HB2 H 2.288 0.03 2 222 . 21 PRO HB3 H 1.770 0.03 2 223 . 21 PRO HG2 H 1.940 0.03 2 224 . 21 PRO HG3 H 1.894 0.03 2 225 . 21 PRO HD2 H 3.628 0.03 2 226 . 21 PRO HD3 H 3.186 0.03 2 227 . 21 PRO CA C 66.547 0.08 1 228 . 21 PRO CB C 30.663 0.08 1 229 . 21 PRO CG C 28.513 0.08 1 230 . 21 PRO CD C 49.504 0.08 1 231 . 22 LYS H H 7.169 0.03 1 232 . 22 LYS HA H 4.181 0.03 1 233 . 22 LYS HB2 H 1.898 0.03 2 234 . 22 LYS HB3 H 1.685 0.03 2 235 . 22 LYS HG2 H 1.274 0.03 2 236 . 22 LYS HG3 H 1.513 0.03 2 237 . 22 LYS HE2 H 3.173 0.03 1 238 . 22 LYS C C 179.404 0.08 1 239 . 22 LYS CA C 58.933 0.08 1 240 . 22 LYS CB C 31.420 0.08 1 241 . 22 LYS CG C 24.596 0.08 4 242 . 22 LYS CD C 29.408 0.08 4 243 . 22 LYS CE C 43.342 0.08 1 244 . 22 LYS N N 115.704 0.08 1 245 . 23 GLN H H 8.075 0.03 1 246 . 23 GLN HA H 4.067 0.03 1 247 . 23 GLN HB2 H 2.307 0.03 2 248 . 23 GLN HB3 H 1.964 0.03 2 249 . 23 GLN HG2 H 2.689 0.03 2 250 . 23 GLN HG3 H 2.107 0.03 2 251 . 23 GLN C C 179.120 0.08 1 252 . 23 GLN CA C 58.016 0.08 1 253 . 23 GLN CB C 28.224 0.08 1 254 . 23 GLN CG C 32.947 0.08 1 255 . 23 GLN N N 118.279 0.08 1 256 . 24 ILE H H 8.845 0.03 1 257 . 24 ILE HA H 3.687 0.03 1 258 . 24 ILE HB H 1.980 0.03 1 259 . 24 ILE HG12 H 1.688 0.03 2 260 . 24 ILE HG13 H 1.055 0.03 2 261 . 24 ILE HG2 H 0.870 0.03 1 262 . 24 ILE HD1 H 0.775 0.03 1 263 . 24 ILE C C 179.501 0.08 1 264 . 24 ILE CA C 66.133 0.08 1 265 . 24 ILE CB C 37.573 0.08 1 266 . 24 ILE CG1 C 30.699 0.08 1 267 . 24 ILE CG2 C 17.197 0.08 1 268 . 24 ILE CD1 C 12.938 0.08 1 269 . 24 ILE N N 124.930 0.08 1 270 . 25 GLU H H 7.531 0.03 1 271 . 25 GLU HA H 4.202 0.03 1 272 . 25 GLU HB2 H 2.188 0.03 2 273 . 25 GLU HG2 H 2.271 0.03 2 274 . 25 GLU HG3 H 2.375 0.03 2 275 . 25 GLU C C 177.743 0.08 1 276 . 25 GLU CA C 59.584 0.08 1 277 . 25 GLU CB C 29.879 0.08 1 278 . 25 GLU CG C 35.893 0.08 1 279 . 25 GLU N N 118.802 0.08 1 280 . 26 ARG H H 8.478 0.03 1 281 . 26 ARG HA H 4.110 0.03 1 282 . 26 ARG HB2 H 1.896 0.03 2 283 . 26 ARG HG2 H 1.751 0.03 2 284 . 26 ARG HD2 H 3.170 0.03 2 285 . 26 ARG C C 180.967 0.08 1 286 . 26 ARG CA C 58.571 0.08 1 287 . 26 ARG CB C 30.387 0.08 1 288 . 26 ARG CG C 27.141 0.08 1 289 . 26 ARG CD C 43.243 0.08 1 290 . 26 ARG N N 119.173 0.08 1 291 . 27 ASN H H 7.424 0.03 1 292 . 27 ASN HA H 4.610 0.03 1 293 . 27 ASN HB2 H 2.766 0.03 2 294 . 27 ASN HB3 H 2.423 0.03 2 295 . 27 ASN C C 177.352 0.08 1 296 . 27 ASN CA C 54.590 0.08 1 297 . 27 ASN CB C 39.913 0.08 1 298 . 27 ASN N N 114.413 0.08 1 299 . 28 ALA H H 7.906 0.03 1 300 . 28 ALA HA H 4.074 0.03 1 301 . 28 ALA HB H 1.425 0.03 1 302 . 28 ALA C C 172.175 0.08 1 303 . 28 ALA CA C 53.462 0.08 1 304 . 28 ALA CB C 16.463 0.08 1 305 . 28 ALA N N 119.020 0.08 1 306 . 29 LEU H H 7.542 0.03 1 307 . 29 LEU HA H 4.340 0.03 1 308 . 29 LEU HB2 H 1.478 0.03 2 309 . 29 LEU HB3 H 1.830 0.03 2 310 . 29 LEU HG H 1.477 0.03 1 311 . 29 LEU HD1 H 0.884 0.03 1 312 . 29 LEU HD2 H 0.910 0.03 1 313 . 29 LEU C C 176.571 0.08 1 314 . 29 LEU CA C 55.227 0.08 1 315 . 29 LEU CB C 43.572 0.08 1 316 . 29 LEU CG C 27.257 0.08 1 317 . 29 LEU CD1 C 24.816 0.08 2 318 . 29 LEU CD2 C 26.961 0.08 2 319 . 29 LEU N N 119.368 0.08 1 320 . 30 LYS H H 8.899 0.03 1 321 . 30 LYS HA H 4.354 0.03 1 322 . 30 LYS HB2 H 1.519 0.03 2 323 . 30 LYS HB3 H 1.906 0.03 2 324 . 30 LYS HG3 H 1.407 0.03 2 325 . 30 LYS HD2 H 1.672 0.03 2 326 . 30 LYS HD3 H 1.676 0.03 2 327 . 30 LYS HE2 H 3.016 0.03 2 328 . 30 LYS CA C 54.891 0.08 1 329 . 30 LYS CB C 33.473 0.08 1 330 . 30 LYS CG C 25.159 0.08 1 331 . 30 LYS CD C 28.843 0.08 1 332 . 30 LYS CE C 42.168 0.08 1 333 . 30 LYS N N 122.254 0.08 1 334 . 31 LYS H H 8.624 0.03 1 335 . 31 LYS HA H 4.016 0.03 1 336 . 31 LYS HB2 H 1.806 0.03 2 337 . 31 LYS HB3 H 1.734 0.03 2 338 . 31 LYS HG2 H 1.392 0.03 2 339 . 31 LYS HG3 H 1.515 0.03 2 340 . 31 LYS HD2 H 1.685 0.03 2 341 . 31 LYS HE2 H 3.013 0.03 2 342 . 31 LYS HE3 H 2.850 0.03 2 343 . 31 LYS CA C 58.605 0.08 1 344 . 31 LYS CB C 31.776 0.08 1 345 . 31 LYS CG C 24.550 0.08 4 346 . 31 LYS CD C 29.225 0.08 4 347 . 31 LYS CE C 42.023 0.08 2 348 . 31 LYS N N 123.150 0.08 2 349 . 32 GLY H H 8.839 0.03 1 350 . 32 GLY HA2 H 4.190 0.03 2 351 . 32 GLY HA3 H 3.750 0.03 2 352 . 32 GLY C C 177.938 0.08 1 353 . 32 GLY CA C 45.161 0.08 1 354 . 32 GLY N N 112.350 0.08 1 355 . 33 GLU H H 8.129 0.03 1 356 . 33 GLU HA H 4.400 0.03 1 357 . 33 GLU HB2 H 1.938 0.03 2 358 . 33 GLU HG2 H 2.264 0.03 2 359 . 33 GLU HG3 H 2.243 0.03 2 360 . 33 GLU C C 175.496 0.08 1 361 . 33 GLU CA C 59.748 0.08 1 362 . 33 GLU CB C 30.413 0.08 1 363 . 33 GLU CG C 38.246 0.08 1 364 . 33 GLU N N 120.945 0.08 1 365 . 34 LEU H H 8.288 0.03 1 366 . 34 LEU HA H 5.126 0.03 1 367 . 34 LEU HB2 H 1.738 0.03 2 368 . 34 LEU HB3 H 0.952 0.03 2 369 . 34 LEU HG H 1.081 0.03 1 370 . 34 LEU HD1 H 0.529 0.03 1 371 . 34 LEU HD2 H 0.601 0.03 1 372 . 34 LEU C C 175.105 0.08 1 373 . 34 LEU CA C 53.483 0.08 1 374 . 34 LEU CB C 45.278 0.08 1 375 . 34 LEU CG C 27.567 0.08 1 376 . 34 LEU CD1 C 23.566 0.08 2 377 . 34 LEU CD2 C 27.260 0.08 2 378 . 34 LEU N N 118.544 0.08 1 379 . 35 THR H H 8.713 0.03 1 380 . 35 THR HA H 4.447 0.03 1 381 . 35 THR HB H 3.945 0.03 1 382 . 35 THR HG2 H 1.240 0.03 1 383 . 35 THR C C 175.399 0.08 1 384 . 35 THR CA C 61.500 0.08 1 385 . 35 THR CB C 71.187 0.08 1 386 . 35 THR CG2 C 21.479 0.08 1 387 . 35 THR N N 123.447 0.08 1 388 . 36 VAL H H 8.871 0.03 1 389 . 36 VAL HA H 4.363 0.03 1 390 . 36 VAL HB H 2.003 0.03 1 391 . 36 VAL HG1 H 0.658 0.03 2 392 . 36 VAL HG2 H 0.631 0.03 2 393 . 36 VAL C C 172.370 0.08 1 394 . 36 VAL CA C 60.868 0.08 1 395 . 36 VAL CB C 32.105 0.08 1 396 . 36 VAL CG1 C 22.110 0.08 2 397 . 36 VAL CG2 C 20.869 0.08 2 398 . 36 VAL N N 127.612 0.08 1 399 . 37 ASP H H 8.766 0.03 1 400 . 37 ASP HA H 4.633 0.03 1 401 . 37 ASP HB2 H 2.823 0.03 2 402 . 37 ASP HB3 H 2.941 0.03 2 403 . 37 ASP C C 174.617 0.08 1 404 . 37 ASP CA C 54.298 0.08 1 405 . 37 ASP CB C 42.302 0.08 1 406 . 37 ASP N N 126.484 0.08 1 407 . 38 ASP H H 9.063 0.03 1 408 . 38 ASP HA H 4.143 0.03 1 409 . 38 ASP HB2 H 2.740 0.03 2 410 . 38 ASP HB3 H 2.589 0.03 2 411 . 38 ASP C C 177.157 0.08 1 412 . 38 ASP CA C 58.318 0.08 1 413 . 38 ASP CB C 39.270 0.08 1 414 . 38 ASP N N 124.410 0.08 1 415 . 39 SER H H 8.603 0.03 1 416 . 39 SER HA H 4.112 0.03 1 417 . 39 SER HB2 H 3.974 0.03 2 418 . 39 SER C C 177.938 0.08 1 419 . 39 SER CA C 61.214 0.08 1 420 . 39 SER CB C 62.582 0.08 1 421 . 39 SER N N 112.865 0.08 1 422 . 40 ALA H H 7.808 0.03 1 423 . 40 ALA HA H 4.066 0.03 1 424 . 40 ALA HB H 1.270 0.03 1 425 . 40 ALA C C 178.134 0.08 1 426 . 40 ALA CA C 54.261 0.08 1 427 . 40 ALA CB C 18.550 0.08 1 428 . 40 ALA N N 125.503 0.08 1 429 . 41 ILE H H 7.241 0.03 1 430 . 41 ILE HA H 3.394 0.03 1 431 . 41 ILE HB H 1.977 0.03 1 432 . 41 ILE HG12 H 0.759 0.03 2 433 . 41 ILE HG13 H 1.654 0.03 2 434 . 41 ILE HG2 H 0.890 0.03 1 435 . 41 ILE HD1 H 0.755 0.03 1 436 . 41 ILE C C 178.134 0.08 1 437 . 41 ILE CA C 65.348 0.08 1 438 . 41 ILE CB C 36.535 0.08 1 439 . 41 ILE CG1 C 28.863 0.08 1 440 . 41 ILE CG2 C 19.037 0.08 1 441 . 41 ILE CD1 C 13.111 0.08 1 442 . 41 ILE N N 117.516 0.08 1 443 . 42 ILE H H 8.553 0.03 1 444 . 42 ILE HA H 3.634 0.03 1 445 . 42 ILE HB H 1.816 0.03 1 446 . 42 ILE HG12 H 1.505 0.03 2 447 . 42 ILE HG13 H 1.290 0.03 2 448 . 42 ILE HG2 H 0.749 0.03 1 449 . 42 ILE HD1 H 0.683 0.03 1 450 . 42 ILE C C 177.938 0.08 1 451 . 42 ILE CA C 63.819 0.08 1 452 . 42 ILE CB C 36.590 0.08 1 453 . 42 ILE CG1 C 28.324 0.08 1 454 . 42 ILE CG2 C 16.566 0.08 1 455 . 42 ILE CD1 C 11.076 0.08 1 456 . 42 ILE N N 119.049 0.08 1 457 . 43 GLY H H 7.664 0.03 1 458 . 43 GLY HA2 H 3.995 0.03 2 459 . 43 GLY HA3 H 3.909 0.03 2 460 . 43 GLY C C 177.645 0.08 1 461 . 43 GLY CA C 47.167 0.08 1 462 . 43 GLY N N 106.985 0.08 1 463 . 44 ILE H H 8.284 0.03 1 464 . 44 ILE HA H 3.942 0.03 1 465 . 44 ILE HB H 2.044 0.03 1 466 . 44 ILE HG12 H 0.551 0.03 2 467 . 44 ILE HG13 H 2.224 0.03 2 468 . 44 ILE HG2 H 0.849 0.03 1 469 . 44 ILE HD1 H 0.610 0.03 1 470 . 44 ILE C C 176.082 0.08 1 471 . 44 ILE CA C 66.259 0.08 1 472 . 44 ILE CB C 38.083 0.08 1 473 . 44 ILE CG1 C 28.722 0.08 1 474 . 44 ILE CG2 C 20.233 0.08 1 475 . 44 ILE CD1 C 13.762 0.08 1 476 . 44 ILE N N 122.323 0.08 1 477 . 45 ILE H H 8.148 0.03 1 478 . 45 ILE HA H 3.424 0.03 1 479 . 45 ILE HB H 1.959 0.03 1 480 . 45 ILE HG12 H 0.900 0.03 2 481 . 45 ILE HG13 H 1.880 0.03 2 482 . 45 ILE HG2 H 0.928 0.03 1 483 . 45 ILE HD1 H 0.779 0.03 1 484 . 45 ILE C C 178.915 0.08 1 485 . 45 ILE CA C 65.370 0.08 1 486 . 45 ILE CB C 38.583 0.08 1 487 . 45 ILE CG1 C 30.227 0.08 1 488 . 45 ILE CG2 C 18.119 0.08 1 489 . 45 ILE CD1 C 15.646 0.08 1 490 . 45 ILE N N 119.570 0.08 1 491 . 46 ARG H H 8.342 0.03 1 492 . 46 ARG HA H 3.849 0.03 1 493 . 46 ARG HB2 H 0.835 0.03 2 494 . 46 ARG HB3 H 0.508 0.03 2 495 . 46 ARG HG2 H 0.856 0.03 2 496 . 46 ARG HG3 H 1.593 0.03 2 497 . 46 ARG HD2 H 2.398 0.03 2 498 . 46 ARG HD3 H 2.014 0.03 2 499 . 46 ARG C C 177.548 0.08 1 500 . 46 ARG CA C 59.772 0.08 1 501 . 46 ARG CB C 31.151 0.08 1 502 . 46 ARG CG C 27.745 0.08 1 503 . 46 ARG CD C 43.334 0.08 1 504 . 46 ARG N N 113.788 0.08 1 505 . 47 TYR H H 8.321 0.03 1 506 . 47 TYR HA H 5.313 0.03 1 507 . 47 TYR HB2 H 2.982 0.03 2 508 . 47 TYR C C 178.232 0.08 1 509 . 47 TYR CA C 57.516 0.08 1 510 . 47 TYR CB C 39.580 0.08 1 511 . 47 TYR N N 111.480 0.08 1 512 . 48 TYR H H 8.304 0.03 1 513 . 48 TYR HA H 4.858 0.03 1 514 . 48 TYR HB2 H 3.413 0.03 2 515 . 48 TYR HB3 H 3.209 0.03 2 516 . 48 TYR C C 177.352 0.08 1 517 . 48 TYR CA C 59.051 0.08 1 518 . 48 TYR CB C 39.872 0.08 1 519 . 48 TYR N N 115.268 0.08 1 520 . 49 THR H H 7.476 0.03 1 521 . 49 THR HA H 4.808 0.03 1 522 . 49 THR HB H 4.016 0.03 1 523 . 49 THR HG2 H 0.990 0.03 1 524 . 49 THR C C 174.422 0.08 1 525 . 49 THR CB C 73.940 0.08 1 526 . 49 THR CG2 C 21.540 0.08 1 527 . 49 THR N N 108.891 0.08 1 528 . 50 ARG H H 8.399 0.03 1 529 . 50 ARG HA H 4.195 0.03 1 530 . 50 ARG HB2 H 1.166 0.03 2 531 . 50 ARG HB3 H 0.551 0.03 2 532 . 50 ARG HG2 H 1.042 0.03 2 533 . 50 ARG HD2 H 2.994 0.03 2 534 . 50 ARG HD3 H 2.845 0.03 2 535 . 50 ARG C C 171.100 0.08 1 536 . 50 ARG CA C 56.156 0.08 1 537 . 50 ARG CB C 29.793 0.08 1 538 . 50 ARG CG C 26.282 0.08 1 539 . 50 ARG CD C 43.340 0.08 1 540 . 50 ARG N N 121.506 0.08 1 541 . 51 GLU H H 8.671 0.03 1 542 . 51 GLU HA H 4.855 0.03 1 543 . 51 GLU HB2 H 2.202 0.03 2 544 . 51 GLU HB3 H 1.988 0.03 2 545 . 51 GLU HG2 H 2.434 0.03 2 546 . 51 GLU HG3 H 2.065 0.03 2 547 . 51 GLU C C 173.640 0.08 1 548 . 51 GLU CA C 54.486 0.08 1 549 . 51 GLU CB C 30.777 0.08 1 550 . 51 GLU CG C 32.893 0.08 1 551 . 51 GLU N N 121.261 0.08 1 552 . 52 ALA H H 8.879 0.03 1 553 . 52 ALA HA H 4.603 0.03 1 554 . 52 ALA HB H 1.432 0.03 1 555 . 52 ALA C C 174.910 0.08 1 556 . 52 ALA CA C 53.462 0.08 1 557 . 52 ALA CB C 19.618 0.08 1 558 . 52 ALA N N 125.755 0.08 1 559 . 53 GLY H H 7.484 0.03 1 560 . 53 GLY HA2 H 4.564 0.03 2 561 . 53 GLY HA3 H 3.888 0.03 2 562 . 53 GLY C C 178.427 0.08 1 563 . 53 GLY CA C 44.237 0.08 1 564 . 53 GLY N N 105.445 0.08 1 565 . 54 VAL H H 8.501 0.03 1 566 . 54 VAL HA H 4.933 0.03 1 567 . 54 VAL HB H 2.631 0.03 1 568 . 54 VAL HG1 H 0.723 0.03 1 569 . 54 VAL HG2 H 0.843 0.03 1 570 . 54 VAL C C 172.370 0.08 1 571 . 54 VAL CA C 60.042 0.08 1 572 . 54 VAL CB C 32.332 0.08 1 573 . 54 VAL CG1 C 22.559 0.08 1 574 . 54 VAL CG2 C 17.795 0.08 1 575 . 54 VAL N N 107.063 0.08 1 576 . 55 ARG H H 7.966 0.03 1 577 . 55 ARG C C 176.766 0.08 1 578 . 55 ARG N N 124.959 0.08 1 579 . 56 GLY HA2 H 3.784 0.03 2 580 . 56 GLY HA3 H 3.639 0.03 2 581 . 56 GLY CA C 46.449 0.08 1 582 . 57 LEU H H 8.878 0.03 1 583 . 57 LEU HA H 3.765 0.03 1 584 . 57 LEU HB2 H 1.899 0.03 2 585 . 57 LEU HB3 H 1.805 0.03 2 586 . 57 LEU HG H 1.411 0.03 1 587 . 57 LEU HD1 H 0.874 0.03 1 588 . 57 LEU HD2 H 0.838 0.03 1 589 . 57 LEU C C 176.962 0.08 1 590 . 57 LEU CA C 58.494 0.08 1 591 . 57 LEU CB C 40.947 0.08 1 592 . 57 LEU CG C 26.694 0.08 1 593 . 57 LEU CD1 C 24.489 0.08 2 594 . 57 LEU CD2 C 26.479 0.08 2 595 . 57 LEU N N 126.397 0.08 1 596 . 58 GLU H H 8.518 0.03 1 597 . 58 GLU HA H 3.640 0.03 1 598 . 58 GLU HB2 H 2.281 0.03 2 599 . 58 GLU HB3 H 2.075 0.03 2 600 . 58 GLU HG2 H 2.357 0.03 2 601 . 58 GLU HG3 H 2.097 0.03 2 602 . 58 GLU C C 177.841 0.08 1 603 . 58 GLU CA C 60.662 0.08 1 604 . 58 GLU CB C 28.935 0.08 1 605 . 58 GLU CG C 36.611 0.08 1 606 . 58 GLU N N 118.166 0.08 1 607 . 59 ARG H H 7.983 0.03 1 608 . 59 ARG HA H 4.059 0.03 1 609 . 59 ARG HB2 H 2.088 0.03 2 610 . 59 ARG HB3 H 2.175 0.03 2 611 . 59 ARG HG2 H 1.561 0.03 2 612 . 59 ARG HG3 H 1.914 0.03 2 613 . 59 ARG HD2 H 3.302 0.03 2 614 . 59 ARG HD3 H 3.308 0.03 2 615 . 59 ARG C C 177.841 0.08 1 616 . 59 ARG CA C 59.781 0.08 1 617 . 59 ARG CB C 29.793 0.08 1 618 . 59 ARG CG C 27.576 0.08 1 619 . 59 ARG CD C 43.293 0.08 1 620 . 59 ARG N N 120.496 0.08 1 621 . 60 GLU H H 8.517 0.03 1 622 . 60 GLU HA H 4.235 0.03 1 623 . 60 GLU HB2 H 2.089 0.03 2 624 . 60 GLU HB3 H 1.896 0.03 2 625 . 60 GLU HG2 H 2.548 0.03 2 626 . 60 GLU HG3 H 2.095 0.03 2 627 . 60 GLU C C 180.060 0.08 1 628 . 60 GLU CA C 58.478 0.08 1 629 . 60 GLU CB C 29.581 0.08 1 630 . 60 GLU CG C 34.965 0.08 1 631 . 60 GLU N N 119.113 0.08 1 632 . 61 ILE H H 8.292 0.03 1 633 . 61 ILE HA H 3.493 0.03 1 634 . 61 ILE HB H 1.971 0.03 1 635 . 61 ILE HG12 H 0.739 0.03 2 636 . 61 ILE HG13 H 1.901 0.03 2 637 . 61 ILE HG2 H 0.772 0.03 1 638 . 61 ILE C C 179.111 0.08 1 639 . 61 ILE CA C 65.954 0.08 1 640 . 61 ILE CB C 37.502 0.08 1 641 . 61 ILE CG1 C 30.604 0.08 1 642 . 61 ILE CG2 C 18.075 0.08 1 643 . 61 ILE CD1 C 14.283 0.08 1 644 . 61 ILE N N 119.457 0.08 1 645 . 62 SER H H 8.679 0.03 1 646 . 62 SER HA H 4.466 0.03 1 647 . 62 SER HB2 H 3.941 0.03 2 648 . 62 SER C C 178.134 0.08 1 649 . 62 SER CA C 61.475 0.08 1 650 . 62 SER CB C 62.539 0.08 1 651 . 62 SER N N 116.487 0.08 1 652 . 63 LYS H H 7.684 0.03 1 653 . 63 LYS HA H 3.916 0.03 1 654 . 63 LYS HB2 H 1.980 0.03 2 655 . 63 LYS HB3 H 1.891 0.03 2 656 . 63 LYS HG2 H 1.603 0.03 2 657 . 63 LYS HG3 H 1.335 0.03 2 658 . 63 LYS HD2 H 1.728 0.03 2 659 . 63 LYS HE2 H 2.894 0.03 2 660 . 63 LYS C C 176.473 0.08 1 661 . 63 LYS CA C 60.201 0.08 1 662 . 63 LYS CB C 32.558 0.08 1 663 . 63 LYS CG C 25.639 0.08 1 664 . 63 LYS CD C 30.085 0.08 1 665 . 63 LYS CE C 41.948 0.08 1 666 . 63 LYS N N 121.089 0.08 1 667 . 64 LEU H H 8.106 0.03 1 668 . 64 LEU HA H 3.833 0.03 1 669 . 64 LEU HB2 H 1.895 0.03 2 670 . 64 LEU HB3 H 1.524 0.03 2 671 . 64 LEU HD1 H 0.647 0.03 1 672 . 64 LEU HD2 H 0.618 0.03 1 673 . 64 LEU C C 179.111 0.08 1 674 . 64 LEU CA C 58.596 0.08 1 675 . 64 LEU CB C 41.744 0.08 1 676 . 64 LEU CD1 C 25.780 0.08 2 677 . 64 LEU CD2 C 24.848 0.08 2 678 . 64 LEU N N 118.789 0.08 1 679 . 65 CYS H H 7.918 0.03 1 680 . 65 CYS HA H 3.806 0.03 1 681 . 65 CYS HB2 H 3.066 0.03 2 682 . 65 CYS HB3 H 2.311 0.03 2 683 . 65 CYS C C 178.329 0.08 1 684 . 65 CYS CA C 64.408 0.08 1 685 . 65 CYS CB C 27.632 0.08 1 686 . 65 CYS N N 115.512 0.08 1 687 . 66 ARG H H 8.186 0.03 1 688 . 66 ARG HA H 3.942 0.03 1 689 . 66 ARG HB2 H 1.930 0.03 2 690 . 66 ARG HG2 H 1.845 0.03 2 691 . 66 ARG HG3 H 1.675 0.03 2 692 . 66 ARG HD2 H 3.222 0.03 2 693 . 66 ARG C C 176.180 0.08 1 694 . 66 ARG CA C 59.542 0.08 1 695 . 66 ARG CB C 30.084 0.08 1 696 . 66 ARG CG C 27.660 0.08 1 697 . 66 ARG CD C 43.556 0.08 1 698 . 66 ARG N N 118.545 0.08 1 699 . 67 LYS H H 8.094 0.03 1 700 . 67 LYS HA H 4.138 0.03 1 701 . 67 LYS HB2 H 2.097 0.03 2 702 . 67 LYS HB3 H 2.109 0.03 2 703 . 67 LYS HG2 H 1.723 0.03 2 704 . 67 LYS HG3 H 1.549 0.03 2 705 . 67 LYS HD2 H 1.719 0.03 2 706 . 67 LYS HE2 H 2.967 0.03 2 707 . 67 LYS C C 179.501 0.08 1 708 . 67 LYS CA C 59.196 0.08 1 709 . 67 LYS CB C 32.417 0.08 1 710 . 67 LYS CG C 26.011 0.08 4 711 . 67 LYS CD C 29.083 0.08 4 712 . 67 LYS CE C 42.131 0.08 1 713 . 67 LYS N N 119.205 0.08 1 714 . 68 ALA H H 8.377 0.03 1 715 . 68 ALA HA H 4.219 0.03 1 716 . 68 ALA HB H 1.395 0.03 1 717 . 68 ALA C C 179.013 0.08 1 718 . 68 ALA CA C 55.551 0.08 1 719 . 68 ALA CB C 18.765 0.08 1 720 . 68 ALA N N 122.588 0.08 1 721 . 69 VAL H H 8.034 0.03 1 722 . 69 VAL HA H 3.644 0.03 1 723 . 69 VAL HB H 2.135 0.03 1 724 . 69 VAL HG1 H 1.185 0.03 2 725 . 69 VAL HG2 H 1.076 0.03 2 726 . 69 VAL C C 178.622 0.08 1 727 . 69 VAL CA C 66.626 0.08 1 728 . 69 VAL CB C 31.927 0.08 1 729 . 69 VAL CG1 C 23.459 0.08 2 730 . 69 VAL CG2 C 20.849 0.08 2 731 . 69 VAL N N 116.318 0.08 1 732 . 70 LYS H H 7.279 0.03 1 733 . 70 LYS HA H 4.021 0.03 1 734 . 70 LYS HB2 H 1.979 0.03 2 735 . 70 LYS HB3 H 1.605 0.03 2 736 . 70 LYS HG2 H 1.511 0.03 2 737 . 70 LYS HG3 H 1.374 0.03 2 738 . 70 LYS HD2 H 1.699 0.03 2 739 . 70 LYS HE2 H 2.983 0.03 2 740 . 70 LYS C C 177.939 0.08 1 741 . 70 LYS CA C 59.237 0.08 1 742 . 70 LYS CB C 32.136 0.08 1 743 . 70 LYS CG C 24.937 0.08 4 744 . 70 LYS CD C 29.118 0.08 4 745 . 70 LYS CE C 42.209 0.08 1 746 . 70 LYS N N 118.503 0.08 1 747 . 71 GLN H H 8.047 0.03 1 748 . 71 GLN HA H 3.984 0.03 1 749 . 71 GLN HB2 H 2.093 0.03 2 750 . 71 GLN HB3 H 2.329 0.03 2 751 . 71 GLN HG2 H 2.557 0.03 2 752 . 71 GLN HG3 H 2.350 0.03 2 753 . 71 GLN CA C 59.258 0.08 1 754 . 71 GLN CB C 28.547 0.08 1 755 . 71 GLN CG C 34.005 0.08 1 756 . 71 GLN N N 118.673 0.08 1 757 . 72 LEU H H 7.996 0.03 1 758 . 72 LEU HA H 4.067 0.03 1 759 . 72 LEU HB2 H 1.898 0.03 2 760 . 72 LEU HB3 H 1.513 0.03 2 761 . 72 LEU HG H 1.740 0.03 1 762 . 72 LEU HD1 H 0.667 0.03 2 763 . 72 LEU HD2 H 0.700 0.03 2 764 . 72 LEU C C 178.915 0.08 1 765 . 72 LEU CA C 57.619 0.08 1 766 . 72 LEU CB C 41.728 0.08 1 767 . 72 LEU CG C 26.739 0.08 1 768 . 72 LEU CD1 C 22.937 0.08 2 769 . 72 LEU CD2 C 26.056 0.08 2 770 . 72 LEU N N 118.620 0.08 1 771 . 73 LEU H H 7.775 0.03 1 772 . 73 LEU HA H 4.111 0.03 1 773 . 73 LEU HB2 H 1.613 0.03 2 774 . 73 LEU HB3 H 1.868 0.03 2 775 . 73 LEU HG H 1.846 0.03 1 776 . 73 LEU HD1 H 0.898 0.03 2 777 . 73 LEU HD2 H 0.905 0.03 2 778 . 73 LEU C C 179.013 0.08 1 779 . 73 LEU CA C 56.898 0.08 1 780 . 73 LEU CB C 42.354 0.08 1 781 . 73 LEU CG C 27.086 0.08 1 782 . 73 LEU CD1 C 24.869 0.08 2 783 . 73 LEU CD2 C 23.358 0.08 2 784 . 73 LEU N N 117.621 0.08 1 785 . 74 LEU H H 7.640 0.03 1 786 . 74 LEU HA H 4.212 0.03 1 787 . 74 LEU HB2 H 1.802 0.03 2 788 . 74 LEU HB3 H 1.600 0.03 2 789 . 74 LEU HG H 1.830 0.03 1 790 . 74 LEU HD1 H 0.891 0.03 1 791 . 74 LEU C C 179.208 0.08 1 792 . 74 LEU CA C 56.324 0.08 1 793 . 74 LEU CB C 42.878 0.08 1 794 . 74 LEU CG C 27.012 0.08 1 795 . 74 LEU CD1 C 24.896 0.08 2 796 . 74 LEU CD2 C 23.301 0.08 2 797 . 74 LEU N N 117.862 0.08 1 798 . 75 ASP H H 7.595 0.03 1 799 . 75 ASP HA H 4.865 0.03 1 800 . 75 ASP HB2 H 3.025 0.03 2 801 . 75 ASP HB3 H 2.470 0.03 2 802 . 75 ASP C C 177.450 0.08 1 803 . 75 ASP CA C 52.471 0.08 1 804 . 75 ASP CB C 40.836 0.08 1 805 . 75 ASP N N 118.288 0.08 1 806 . 76 LYS H H 8.471 0.03 1 807 . 76 LYS HA H 4.412 0.03 1 808 . 76 LYS HB2 H 1.847 0.03 2 809 . 76 LYS HB3 H 1.992 0.03 2 810 . 76 LYS HG2 H 1.816 0.03 2 811 . 76 LYS HG3 H 1.730 0.03 2 812 . 76 LYS HD2 H 1.560 0.03 2 813 . 76 LYS HD3 H 1.633 0.03 2 814 . 76 LYS HE2 H 3.069 0.03 2 815 . 76 LYS C C 175.594 0.08 1 816 . 76 LYS CA C 57.364 0.08 1 817 . 76 LYS CB C 31.597 0.08 1 818 . 76 LYS CG C 28.816 0.08 4 819 . 76 LYS CD C 24.865 0.08 4 820 . 76 LYS CE C 42.340 0.08 1 821 . 76 LYS N N 121.629 0.08 1 822 . 77 SER H H 8.507 0.03 1 823 . 77 SER HA H 4.392 0.03 1 824 . 77 SER HB2 H 4.005 0.03 2 825 . 77 SER HB3 H 3.879 0.03 2 826 . 77 SER C C 177.548 0.08 1 827 . 77 SER CA C 59.473 0.08 1 828 . 77 SER CB C 64.042 0.08 1 829 . 77 SER N N 114.690 0.08 1 830 . 78 LEU H H 7.542 0.03 1 831 . 78 LEU HA H 4.253 0.03 1 832 . 78 LEU HB2 H 1.695 0.03 2 833 . 78 LEU HB3 H 1.631 0.03 2 834 . 78 LEU HG H 1.488 0.03 1 835 . 78 LEU HD1 H 0.842 0.03 1 836 . 78 LEU HD2 H 0.958 0.03 1 837 . 78 LEU C C 174.617 0.08 1 838 . 78 LEU CA C 55.659 0.08 1 839 . 78 LEU CB C 43.082 0.08 1 840 . 78 LEU CG C 26.696 0.08 1 841 . 78 LEU CD1 C 24.553 0.08 2 842 . 78 LEU CD2 C 24.242 0.08 2 843 . 78 LEU N N 125.388 0.08 1 844 . 79 LYS H H 8.661 0.03 1 845 . 79 LYS HA H 4.333 0.03 1 846 . 79 LYS HB2 H 1.798 0.03 2 847 . 79 LYS HB3 H 1.683 0.03 2 848 . 79 LYS HG2 H 1.404 0.03 2 849 . 79 LYS HG3 H 1.370 0.03 2 850 . 79 LYS HD2 H 1.615 0.03 2 851 . 79 LYS HD3 H 1.666 0.03 2 852 . 79 LYS HE2 H 2.984 0.03 2 853 . 79 LYS C C 176.766 0.08 1 854 . 79 LYS CA C 56.440 0.08 1 855 . 79 LYS CB C 33.245 0.08 1 856 . 79 LYS CG C 24.568 0.08 4 857 . 79 LYS CD C 28.526 0.08 4 858 . 79 LYS CE C 42.311 0.08 1 859 . 79 LYS N N 118.544 0.08 1 860 . 80 HIS H H 7.771 0.03 1 861 . 80 HIS HA H 5.256 0.03 1 862 . 80 HIS HB2 H 3.175 0.03 2 863 . 80 HIS HB3 H 3.099 0.03 2 864 . 80 HIS C C 176.473 0.08 1 865 . 80 HIS CA C 54.488 0.08 1 866 . 80 HIS CB C 30.885 0.08 1 867 . 80 HIS N N 116.078 0.08 1 868 . 81 ILE H H 8.597 0.03 1 869 . 81 ILE HA H 4.141 0.03 1 870 . 81 ILE HB H 1.609 0.03 1 871 . 81 ILE HG12 H 1.139 0.03 2 872 . 81 ILE HG13 H 1.389 0.03 2 873 . 81 ILE HG2 H 0.676 0.03 1 874 . 81 ILE HD1 H 0.848 0.03 1 875 . 81 ILE C C 176.165 0.08 1 876 . 81 ILE CA C 60.128 0.08 1 877 . 81 ILE CB C 40.895 0.08 1 878 . 81 ILE CG1 C 27.763 0.08 1 879 . 81 ILE CG2 C 17.630 0.08 1 880 . 81 ILE CD1 C 14.111 0.08 1 881 . 81 ILE N N 125.205 0.08 1 882 . 82 GLU H H 8.372 0.03 1 883 . 82 GLU HA H 5.108 0.03 1 884 . 82 GLU HB2 H 1.828 0.03 2 885 . 82 GLU HB3 H 1.946 0.03 2 886 . 82 GLU HG2 H 2.080 0.03 2 887 . 82 GLU HG3 H 1.939 0.03 2 888 . 82 GLU C C 173.542 0.08 1 889 . 82 GLU CA C 54.277 0.08 1 890 . 82 GLU CB C 31.354 0.08 1 891 . 82 GLU CG C 35.388 0.08 1 892 . 82 GLU N N 127.163 0.08 1 893 . 83 ILE H H 8.693 0.03 1 894 . 83 ILE HA H 4.648 0.03 1 895 . 83 ILE HB H 1.510 0.03 1 896 . 83 ILE HG12 H 1.072 0.03 2 897 . 83 ILE HG13 H 0.486 0.03 2 898 . 83 ILE HG2 H 0.695 0.03 1 899 . 83 ILE HD1 H -0.130 0.03 1 900 . 83 ILE C C 175.105 0.08 1 901 . 83 ILE CA C 59.742 0.08 1 902 . 83 ILE CB C 38.989 0.08 1 903 . 83 ILE CG1 C 27.315 0.08 1 904 . 83 ILE CG2 C 16.970 0.08 1 905 . 83 ILE CD1 C 12.902 0.08 1 906 . 83 ILE N N 126.320 0.08 1 907 . 84 ASN H H 9.619 0.03 1 908 . 84 ASN HA H 4.815 0.03 1 909 . 84 ASN HB2 H 3.075 0.03 2 910 . 84 ASN HB3 H 2.892 0.03 2 911 . 84 ASN C C 173.933 0.08 1 912 . 84 ASN CA C 51.702 0.08 1 913 . 84 ASN CB C 40.804 0.08 1 914 . 84 ASN N N 125.485 0.08 1 915 . 85 GLY H H 8.490 0.03 1 916 . 85 GLY HA2 H 3.732 0.03 2 917 . 85 GLY HA3 H 3.953 0.03 2 918 . 85 GLY C C 174.910 0.08 1 919 . 85 GLY CA C 47.673 0.08 1 920 . 85 GLY N N 103.755 0.08 1 921 . 86 ASP H H 8.224 0.03 1 922 . 86 ASP HA H 4.734 0.03 1 923 . 86 ASP HB2 H 2.763 0.03 2 924 . 86 ASP C C 175.301 0.08 1 925 . 86 ASP CA C 56.455 0.08 1 926 . 86 ASP CB C 41.101 0.08 1 927 . 86 ASP N N 119.608 0.08 1 928 . 87 ASN H H 8.016 0.03 1 929 . 87 ASN HA H 4.809 0.03 1 930 . 87 ASN HB2 H 3.523 0.03 2 931 . 87 ASN HB3 H 2.812 0.03 2 932 . 87 ASN C C 177.352 0.08 1 933 . 87 ASN CA C 52.177 0.08 1 934 . 87 ASN CB C 38.319 0.08 1 935 . 87 ASN N N 115.309 0.08 1 936 . 88 LEU H H 7.547 0.03 1 937 . 88 LEU HA H 3.980 0.03 1 938 . 88 LEU HB2 H 2.007 0.03 2 939 . 88 LEU HB3 H 1.932 0.03 2 940 . 88 LEU HG H 1.098 0.03 1 941 . 88 LEU HD1 H 0.851 0.03 1 942 . 88 LEU C C 177.938 0.08 1 943 . 88 LEU CA C 58.828 0.08 1 944 . 88 LEU CB C 42.751 0.08 1 945 . 88 LEU CG C 26.133 0.08 1 946 . 88 LEU CD1 C 23.821 0.08 2 947 . 88 LEU N N 122.167 0.08 1 948 . 89 HIS H H 8.907 0.03 1 949 . 89 HIS HA H 4.596 0.03 1 950 . 89 HIS HB2 H 3.252 0.03 2 951 . 89 HIS HB3 H 3.193 0.03 2 952 . 89 HIS C C 179.892 0.08 1 953 . 89 HIS CA C 57.583 0.08 1 954 . 89 HIS CB C 27.260 0.08 1 955 . 89 HIS N N 114.250 0.08 1 956 . 90 ASP H H 7.683 0.03 1 957 . 90 ASP HA H 4.178 0.03 1 958 . 90 ASP HB2 H 2.638 0.03 2 959 . 90 ASP HB3 H 2.228 0.03 2 960 . 90 ASP C C 176.766 0.08 1 961 . 90 ASP CA C 56.705 0.08 1 962 . 90 ASP CB C 39.386 0.08 1 963 . 90 ASP N N 122.205 0.08 1 964 . 91 TYR H H 7.581 0.03 1 965 . 91 TYR HA H 4.143 0.03 1 966 . 91 TYR HB2 H 2.767 0.03 2 967 . 91 TYR HB3 H 2.712 0.03 2 968 . 91 TYR CA C 60.303 0.08 1 969 . 91 TYR CB C 41.115 0.08 1 970 . 91 TYR N N 115.838 0.08 1 971 . 92 LEU H H 7.833 0.03 1 972 . 92 LEU HA H 4.444 0.03 1 973 . 92 LEU HB2 H 1.241 0.03 2 974 . 92 LEU HB3 H 0.978 0.03 2 975 . 92 LEU HG H 1.321 0.03 1 976 . 92 LEU HD1 H 0.315 0.03 1 977 . 92 LEU HD2 H 0.767 0.03 1 978 . 92 LEU C C 176.180 0.08 1 979 . 92 LEU CA C 54.141 0.08 1 980 . 92 LEU CB C 43.264 0.08 1 981 . 92 LEU CG C 26.512 0.08 1 982 . 92 LEU CD1 C 25.625 0.08 2 983 . 92 LEU CD2 C 21.656 0.08 2 984 . 92 LEU N N 114.421 0.08 1 985 . 93 GLY H H 7.783 0.03 1 986 . 93 GLY HA2 H 4.399 0.03 2 987 . 93 GLY HA3 H 3.906 0.03 2 988 . 93 GLY C C 177.059 0.08 1 989 . 93 GLY CA C 44.064 0.08 1 990 . 93 GLY N N 108.520 0.08 1 991 . 94 VAL H H 8.375 0.03 1 992 . 94 VAL HA H 3.913 0.03 1 993 . 94 VAL HB H 2.023 0.03 1 994 . 94 VAL HG1 H 0.980 0.03 2 995 . 94 VAL HG2 H 0.682 0.03 2 996 . 94 VAL C C 173.542 0.08 1 997 . 94 VAL CA C 62.898 0.08 1 998 . 94 VAL CB C 32.072 0.08 1 999 . 94 VAL CG1 C 20.583 0.08 2 1000 . 94 VAL CG2 C 21.919 0.08 2 1001 . 94 VAL N N 120.139 0.08 1 1002 . 95 GLN H H 8.442 0.03 1 1003 . 95 GLN HA H 3.144 0.03 1 1004 . 95 GLN HB2 H 1.885 0.03 2 1005 . 95 GLN HB3 H 1.776 0.03 2 1006 . 95 GLN HG2 H 2.313 0.03 2 1007 . 95 GLN HG3 H 2.069 0.03 2 1008 . 95 GLN C C 175.887 0.08 1 1009 . 95 GLN CA C 57.258 0.08 1 1010 . 95 GLN CB C 28.417 0.08 1 1011 . 95 GLN CG C 33.383 0.08 1 1012 . 95 GLN N N 122.885 0.08 1 1013 . 96 ARG H H 6.784 0.03 1 1014 . 96 ARG HA H 4.019 0.03 1 1015 . 96 ARG HB2 H 1.344 0.03 2 1016 . 96 ARG HB3 H 1.187 0.03 2 1017 . 96 ARG HG2 H 1.476 0.03 2 1018 . 96 ARG HG3 H 1.192 0.03 2 1019 . 96 ARG HD2 H 3.125 0.03 2 1020 . 96 ARG HD3 H 3.087 0.03 2 1021 . 96 ARG C C 175.301 0.08 1 1022 . 96 ARG CA C 56.763 0.08 1 1023 . 96 ARG CB C 32.662 0.08 1 1024 . 96 ARG CG C 27.567 0.08 1 1025 . 96 ARG CD C 43.309 0.08 1 1026 . 96 ARG N N 121.119 0.08 1 1027 . 97 PHE H H 7.982 0.03 1 1028 . 97 PHE HA H 4.772 0.03 1 1029 . 97 PHE HB2 H 3.255 0.03 2 1030 . 97 PHE HB3 H 2.520 0.03 2 1031 . 97 PHE C C 175.203 0.08 1 1032 . 97 PHE CA C 56.431 0.08 1 1033 . 97 PHE CB C 42.259 0.08 1 1034 . 97 PHE N N 117.152 0.08 1 1035 . 98 ASP H H 8.541 0.03 1 1036 . 98 ASP HA H 4.852 0.03 1 1037 . 98 ASP HB2 H 2.730 0.03 2 1038 . 98 ASP HB3 H 2.602 0.03 2 1039 . 98 ASP C C 174.422 0.08 1 1040 . 98 ASP CA C 53.365 0.08 1 1041 . 98 ASP CB C 41.711 0.08 1 1042 . 98 ASP N N 119.801 0.08 1 1043 . 99 TYR H H 8.240 0.03 1 1044 . 99 TYR HA H 4.511 0.03 1 1045 . 99 TYR HB2 H 2.839 0.03 2 1046 . 99 TYR HB3 H 2.810 0.03 2 1047 . 99 TYR C C 175.594 0.08 1 1048 . 99 TYR CA C 58.550 0.08 1 1049 . 99 TYR CB C 40.169 0.08 1 1050 . 99 TYR N N 122.003 0.08 1 1051 . 100 GLY H H 8.240 0.03 1 1052 . 100 GLY HA2 H 3.832 0.03 2 1053 . 100 GLY HA3 H 3.652 0.03 2 1054 . 100 GLY C C 175.887 0.08 1 1055 . 100 GLY CA C 45.261 0.08 1 1056 . 100 GLY N N 113.532 0.08 1 1057 . 101 ARG H H 7.645 0.03 1 1058 . 101 ARG CA C 57.182 0.08 1 1059 . 101 ARG CB C 31.477 0.08 1 1060 . 101 ARG N N 125.216 0.08 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 110 109 '168,167' '242,241' '346,345' '711,710' '744,743' '819,818' '857,856' stop_ save_